ArticleJournal of molecular biology2010
Mapping of drebrin binding site on F-actin.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 53 citations in OpenAlex.
- Structural mechanisms of drebrin-mediated F-actin network modulation.Nature communications · 2026Article
- Resonance assignment of the intrinsically disordered actin-binding region of Drebrin.Biomolecular NMR assignments · 2025Article
- Functional Differences Between Neuronal and Non-neuronal Isoforms of Drebrin.Journal of molecular biology · 2025Article
- Drebrin controls scar formation and astrocyte reactivity upon traumatic brain injury by regulating membrane trafficking.Nature communications · 2021Article
- Biased localization of actin binding proteins by actin filament conformation.Nature communications · 2020Article
- Direct Visualization of Actin Filaments and Actin-Binding Proteins in Neuronal Cells.Frontiers in cell and developmental biology · 2020Review
- Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly.Molecular biology of the cell · 2019Article
- Drebrin Isoforms Critically Regulate NMDAR- and mGluR-Dependent LTD Induction.Frontiers in cellular neuroscience · 2018Article
- Connexin43 Forms Supramolecular Complexes through Non-Overlapping Binding Sites for Drebrin, Tubulin, and ZO-1.PloS one · 2016Article
- Septin 9 Exhibits Polymorphic Binding to F-Actin and Inhibits Myosin and Cofilin Activity.Journal of molecular biology · 2015Article
- Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments.Nature structural & molecular biology · 2014Article
- Drebrin inhibits cofilin-induced severing of F-actin.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Article
- Drebrin contains a cryptic F-actin-bundling activity regulated by Cdk5 phosphorylation.The Journal of cell biology · 2013Article
- Drebrin-induced stabilization of actin filaments.The Journal of biological chemistry · 2013Article
- PakB binds to the SH3 domain of Dictyostelium Abp1 and regulates its effects on cell polarity and early development.Molecular biology of the cell · 2013Article
- ATP and ADP actin states.Biopolymers · 2013Article
- Molecular cooperativity of drebrin1-300 binding and structural remodeling of F-actin.Biophysical journal · 2012Article
- Drebrin controls neuronal migration through the formation and alignment of the leading process.Molecular and cellular neurosciences · 2012Article
- Putting structure into context: fitting of atomic models into electron microscopic and electron tomographic reconstructions.Current opinion in cell biology · 2012Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Drebrin is a filament-binding protein involved in organizing the dendritic pool of actin. Previous in vivo studies identified the actin-binding domain of drebrin (DrABD), which causes the same rearrangements in the cytoskeleton as the full-length protein. Site-directed mutagenesis, electron microscopic reconstruction, and chemical cross-linking combined with mass spectrometry analysis were employed here to map the DrABD binding interface on actin filaments. DrABD could be simultaneously attached to two adjacent actin protomers using the combination of 2-iminothiolane (Traut's reagent) and MTS1 [1,1-methanediyl bis(methanethiosulfonate)]. Site-directed mutagenesis combined with chemical cross-linking revealed that residue 238 of DrABD is located within 5.4 A from C374 of actin protomer 1 and that native cysteine 308 of drebrin is near C374 of actin protomer 2. Mass spectrometry analysis revealed that a zero-length cross-linker, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide, can link the N-terminal G-S extension of the recombinant DrABD to E99 and/or E100 on actin. Efficient cross-linking of drebrin residues 238, 248, 252, 270, and 271 to actin residue 51 was achieved with reagents of different lengths (5.4-19 A). These results suggest that the "core" DrABD is centered on actin subdomain 2 and may adopt a folded conformation upon binding to F-actin. The results of electron microscopic reconstruction, which are in a good agreement with the cross-linking data, revealed polymorphism in DrABD binding to F-actin and suggested the existence of two binding sites. These results provide new structural insight into the previously observed competition between drebrin and several other F-actin-binding proteins.
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